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  1. Book ; Online ; Thesis: Effects of N-terminal mutations of human androgen receptor on polyglutamine toxicity

    Funderburk, Sarah F.

    (Wissenschaftliche Berichte des Forschungszentrums Karlsruhe ; 7421)

    2008  

    Author's details Sarah F. Funderburk
    Series title Wissenschaftliche Berichte des Forschungszentrums Karlsruhe ; 7421
    Wissenschaftliche Berichte / Forschungszentrum Karlsruhe
    Collection Wissenschaftliche Berichte / Forschungszentrum Karlsruhe
    Subject code 616.744
    Language English
    Publisher Forschungszentrum Karlsruhe
    Publishing place Karlsruhe
    Publishing country Germany
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Hohenheim, Univ., Diss., 2008
    HBZ-ID HT016354660
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book ; Thesis: Effects of N-terminal mutations of human androgen receptor on polyglutamine toxicity

    Funderburk, Sarah F

    (Wissenschaftliche Berichte / Forschungszentrum Karlsruhe in der Helmholtz-Gemeinschaft ; 7421)

    2008  

    Author's details Sarah F. Funderburk
    Series title Wissenschaftliche Berichte / Forschungszentrum Karlsruhe in der Helmholtz-Gemeinschaft ; 7421
    Language English
    Size XIV, 130 S., graph. Darst.
    Publisher Forschungszentrum Karlsruhe
    Publishing place Karlsruhe
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--Hohenheim, 2008
    Note Auch als elektronische Ressource vorh. ; Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  3. Book ; Online ; Thesis: Effects of N-terminal mutations of human androgen receptor on polyglutamine toxicity

    Funderburk, Sarah F

    (Wissenschaftliche Berichte des Forschungszentrums Karlsruhe ; 7421)

    2008  

    Author's details Sarah F. Funderburk
    Series title Wissenschaftliche Berichte des Forschungszentrums Karlsruhe ; 7421
    Language English
    Size Online-Ressource (152 S., 3,60 MB)
    Publisher Technische Informationsbibliothek u. Universitätsbibliothek ; Forschungszentrum Karlsruhe
    Publishing place Hannover ; Karlsruhe
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss--Hohenheim, 2008
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

    Full text online

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  4. Book ; Online ; Thesis: Effects of N-terminal mutations of human androgen receptor on polyglutamine toxicity

    Funderburk, Sarah F

    (Wissenschaftliche Berichte / Forschungszentrum ; 7421)

    2008  

    Title variant Effekte N-terminaler Mutationen des humanen Androgenrezeptors auf die Polyglutamintoxizität
    Author's details Sarah F. Funderburk
    Series title Wissenschaftliche Berichte / Forschungszentrum <Karlruhe> ; 7421
    Language English
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss--Hohenheim, 2008
    Database Former special subject collection: coastal and deep sea fishing

    Full text online

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  5. Book ; Online ; Thesis: Effects of N-terminal mutations of human androgen receptor on polyglutamine toxicity

    Funderburk, Sarah F. [Verfasser]

    2008  

    Author's details Sarah F. Funderburk
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language English
    Publisher Forschungszentrum Karlsruhe
    Publishing place Karlsruhe
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  6. Article ; Online: The Beclin 1-VPS34 complex--at the crossroads of autophagy and beyond.

    Funderburk, Sarah F / Wang, Qing Jun / Yue, Zhenyu

    Trends in cell biology

    2010  Volume 20, Issue 6, Page(s) 355–362

    Abstract: An increasing body of research on autophagy provides overwhelming evidence for its connection to diverse biological functions and human diseases. Beclin 1, the first mammalian autophagy protein to be described, appears to act as a nexus point between ... ...

    Abstract An increasing body of research on autophagy provides overwhelming evidence for its connection to diverse biological functions and human diseases. Beclin 1, the first mammalian autophagy protein to be described, appears to act as a nexus point between autophagy, endosomal, and perhaps also cell death pathways. Beclin 1 performs these roles as part of a core complex that contains vacuolar sorting protein 34 (VPS34), a class III phosphatidylinositol-3 kinase. The precise mechanism of Beclin 1-mediated regulation of these cellular functions is unclear, but substantial progress has recently been made in identifying new players and their functions in Beclin 1-VSP34 complexes. Here we review emerging studies that are beginning to unveil the physiological functions of Beclin 1-VPS34 in the central control of autophagic activity and other trafficking events through the formation of distinct Beclin 1-VPS34 protein complexes.
    MeSH term(s) Animals ; Apoptosis Regulatory Proteins/metabolism ; Autophagy ; Humans ; Membrane Proteins/metabolism ; Multiprotein Complexes/metabolism ; Phosphatidylinositol 3-Kinases/metabolism
    Chemical Substances Apoptosis Regulatory Proteins ; Membrane Proteins ; Multiprotein Complexes ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
    Language English
    Publishing date 2010-03-29
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2010.03.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Cell "self-eating" (autophagy) mechanism in Alzheimer's disease.

    Funderburk, Sarah F / Marcellino, Bridget K / Yue, Zhenyu

    The Mount Sinai journal of medicine, New York

    2010  Volume 77, Issue 1, Page(s) 59–68

    Abstract: The autophagy pathway is the major degradation pathway of the cell for long-lived proteins and organelles. Dysfunction of autophagy has been linked to several neurodegenerative disorders that are associated with an accumulation of misfolded protein ... ...

    Abstract The autophagy pathway is the major degradation pathway of the cell for long-lived proteins and organelles. Dysfunction of autophagy has been linked to several neurodegenerative disorders that are associated with an accumulation of misfolded protein aggregates. Alzheimer's disease, the most common neurodegenerative disorder, is characterized by 2 aggregate forms, tau tangles and amyloid-beta plaques. Autophagy has been linked to Alzheimer's disease pathogenesis through its merger with the endosomal-lysosomal system, which has been shown to play a role in the formation of the latter amyloid-beta plaques. However, the precise role of autophagy in Alzheimer's disease pathogenesis is still under contention. One hypothesis is that aberrant autophagy induction results in an accumulation of autophagic vacuoles containing amyloid-beta and the components necessary for its generation, whereas other evidence points to impaired autophagic clearance or even an overall reduction in autophagic activity playing a role in Alzheimer's disease pathogenesis. In this review, we discuss the current evidence linking autophagy to Alzheimer's disease as well as the uncertainty over the exact role and level of autophagic regulation in the pathogenic mechanism of Alzheimer's disease.
    MeSH term(s) Alzheimer Disease/physiopathology ; Amyloid beta-Peptides/metabolism ; Animals ; Autophagy ; Disease Models, Animal ; Humans ; Mice ; Mice, Transgenic ; Models, Biological
    Chemical Substances Amyloid beta-Peptides
    Language English
    Publishing date 2010-01-25
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 130499-9
    ISSN 1931-7581 ; 0027-2507
    ISSN (online) 1931-7581
    ISSN 0027-2507
    DOI 10.1002/msj.20161
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Book ; Online ; Thesis: Effects of N-terminal mutations of human androgen receptor on polyglutamine toxicity

    Funderburk, Sarah F. [Verfasser] / Cato, Andrew C. B. [Akademischer Betreuer]

    2008  

    Author's details Sarah F. Funderburk. Betreuer: Andrew C. B. Cato
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language English
    Publisher Kommunikations-, Informations- und Medienzentrum der Universität Hohenheim
    Publishing place Hohenheim
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

    Full text online

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  9. Article ; Online: Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG.

    Li, Xiaohua / He, Liqiang / Che, Ka Hing / Funderburk, Sarah F / Pan, Lifeng / Pan, Nina / Zhang, Mingjie / Yue, Zhenyu / Zhao, Yanxiang

    Nature communications

    2012  Volume 3, Page(s) 662

    Abstract: Beclin 1 is a core component of the Class III Phosphatidylinositol 3-Kinase VPS34 complex. The coiled coil domain of Beclin 1 serves as an interaction platform for assembly of distinct Atg14L- and UVRAG-containing complexes to modulate VPS34 activity. ... ...

    Abstract Beclin 1 is a core component of the Class III Phosphatidylinositol 3-Kinase VPS34 complex. The coiled coil domain of Beclin 1 serves as an interaction platform for assembly of distinct Atg14L- and UVRAG-containing complexes to modulate VPS34 activity. Here we report the crystal structure of the coiled coil domain that forms an antiparallel dimer and is rendered metastable by a series of 'imperfect' a-d' pairings at its coiled coil interface. Atg14L and UVRAG promote the transition of metastable homodimeric Beclin 1 to heterodimeric Beclin1-Atg14L/UVRAG assembly. Beclin 1 mutants with their 'imperfect' a-d' pairings modified to enhance self-interaction, show distinctively altered interactions with Atg14L or UVRAG. These results suggest that specific utilization of the dimer interface and modulation of the homodimer-heterodimer transition by Beclin 1-interacting partners may underlie the molecular mechanism that controls the formation of various Beclin1-VPS34 subcomplexes to exert their effect on an array of VPS34-related activities, including autophagy.
    MeSH term(s) Adaptor Proteins, Vesicular Transport/chemistry ; Amino Acid Motifs ; Amino Acid Sequence ; Apoptosis Regulatory Proteins/metabolism ; Autophagy ; Autophagy-Related Proteins ; Beclin-1 ; Class III Phosphatidylinositol 3-Kinases/chemistry ; Crystallography, X-Ray/methods ; Dimerization ; HEK293 Cells ; Humans ; Membrane Proteins/metabolism ; Models, Molecular ; Molecular Conformation ; Molecular Sequence Data ; Mutation ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Static Electricity ; Temperature ; Tumor Suppressor Proteins/chemistry
    Chemical Substances ATG14 protein, human ; Adaptor Proteins, Vesicular Transport ; Apoptosis Regulatory Proteins ; Autophagy-Related Proteins ; BECN1 protein, human ; Beclin-1 ; Membrane Proteins ; Tumor Suppressor Proteins ; UVRAG protein, human ; Class III Phosphatidylinositol 3-Kinases (EC 2.7.1.137)
    Language English
    Publishing date 2012-02-07
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/ncomms1648
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Specific N-terminal mutations in the human androgen receptor induce cytotoxicity.

    Funderburk, Sarah F / Shatkina, Liubov / Mink, Sigrun / Weis, Qun / Weg-Remers, Susanne / Cato, Andrew C B

    Neurobiology of aging

    2009  Volume 30, Issue 11, Page(s) 1851–1864

    Abstract: Polyglutamine (polyQ) stretch amplification in different proteins causes neurodegenerative disease. These proteins form intracellular aggregates thought to be cytotoxic but differ in pathology and tissue specificity. Here, we demonstrate that specific ... ...

    Abstract Polyglutamine (polyQ) stretch amplification in different proteins causes neurodegenerative disease. These proteins form intracellular aggregates thought to be cytotoxic but differ in pathology and tissue specificity. Here, we demonstrate that specific sequences outside the polyQ stretch of the human androgen receptor contribute to polyQ pathology. An exchange of two N-terminal serine phosphorylation residues to alanine in the wild type androgen receptor (ARQ22dm) resulted in cytoplasmic accumulation and increased early hormone-dependent aggregation of the receptor. In a Drosophila model, the ARQ22dm was cytotoxic, and developing larvae expressing this receptor showed behavioral abnormalities and severely impaired locomotion. In contrast, the same double mutation in an androgen receptor with an extended polyQ stretch was less toxic. The response of the receptors to inhibitors of polyglutamine toxicity is altered by the amino acid exchanges suggesting that careful consideration is needed in the choice of potential therapies of disorders involving toxic polyQ species.
    MeSH term(s) Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Behavioral Symptoms/genetics ; Behavioral Symptoms/pathology ; Butyrates/pharmacology ; COS Cells ; Cercopithecus aethiops ; Disease Models, Animal ; Drosophila ; Drosophila Proteins/genetics ; Humans ; Larva ; Locomotion/drug effects ; Locomotion/genetics ; Melatonin/pharmacology ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Muscular Atrophy, Spinal/genetics ; Muscular Atrophy, Spinal/metabolism ; Muscular Atrophy, Spinal/mortality ; Muscular Atrophy, Spinal/physiopathology ; Mutation/genetics ; Peptide Fragments/genetics ; Receptors, Androgen/chemistry ; Receptors, Androgen/genetics ; Serine/genetics ; Survival Analysis ; Transfection/methods ; Trinucleotide Repeats/genetics
    Chemical Substances Butyrates ; Drosophila Proteins ; Peptide Fragments ; Receptors, Androgen ; Serine (452VLY9402) ; Mitogen-Activated Protein Kinase Kinases (EC 2.7.12.2) ; Melatonin (JL5DK93RCL)
    Language English
    Publishing date 2009-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 604505-4
    ISSN 1558-1497 ; 0197-4580
    ISSN (online) 1558-1497
    ISSN 0197-4580
    DOI 10.1016/j.neurobiolaging.2007.12.023
    Database MEDical Literature Analysis and Retrieval System OnLINE

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